Browsing by Author "Yasid, NA"
Now showing 1 - 2 of 2
Results Per Page
Sort Options
- Some of the metrics are blocked by yourconsent settings
Publication An alternative bioassay using Anabas testudineus (Climbing perch) colinesterase for metal ions detection(Univ Putra Malaysia Press, 2016) ;Ahmad, SA ;Wong, YF ;Shukor, MY ;Sabullah, MK ;Yasid, NA ;Hayat, NM ;Shamaan, NA ;Khalid, ASyed, MAClimbing Perch or its scientific name, Anabas testudineus is one of the freshwater fish belonging to the family of Anabantidae. It is widely distributed in ponds, swamps and estuaries in Asia. In this study, cholinesterase (ChE) was partially purified from the liver of A. testudineus through ion exchange chromatography. This purification method provided a recovery yield of 5.36% with a purification fold of 6.6. The optimum conditions for ChE assay were identified to be 2.5 mM of butyrylthiocholine iodide (BTC) with pH 8.0 in Tris-HCl buffer at 40 degrees C. Substrate specificity profile also indicated that ChE favours BTC as substrate because it records the highest catalytic efficiency (V-max/K-m). Protein analysis through Native-PAGE showed that ion exchange chromatography is an effective method to partially purify ChE. Metal ion inhibition tests were conducted and mercury (Hg) was found to show the highest inhibition effect (87.30%) whereas lead (Pb) shows the lowest inhibition effect (28.01%). All these findings showed that partially purified ChE from the liver of A. testudineus is suitable to be used as a bioindicator to detect the presence of metal ions. (c) All Rights Reserved - Some of the metrics are blocked by yourconsent settings
Publication Evaluation Of Cholinesterase From The Muscle And Blood Of Anabas Testudineus As Detection Of Metal Ions(Parlar Scientific Publications (P S P), 2016) ;Ahmad, SA ;Sabullah, MK ;Basirun, AA ;Khalid, A ;Yasid, NA ;Iqbal, IM ;Shamaan, NA ;Syed, MAShukor, MYAnother alternative source of cholinesterase (ChE) that is sensitive towards metal ion has been revealed. ChE from muscle and blood of Anabas testudineus were extracted and purified through ammonium sulphate precipitation followed by an ion exchange chromatography with a total recovery of 47.66% and 7.92%, respectively. Kinetic study measured that BTC was the most preferable synthetic substrate to blood ChE while muscle ChE preferred PTC with the biomolecular constant of 1.07 and 0.53 mM, respectively. Optimum pH for blood and muscle ChE were determined at 8 and 9. Both ChE shared an optimum temperature of 30 degrees C. Inhibition study showed that muscle ChE has inhibited more than 50% of metal ions namely arsenic, chromium, copper, mercury and zinc compared to blood ChE with only copper and mercury. Studies on half inhibitory effect (IC50) of blood and muscle ChE were tested with series concentration of mercury calculated at 1.003 and 1.048 mg/L. This result will be used as a reference for future development of biosensor.